Cat: IPD-X25753

Recombinant Human ARF5 Protein,His

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Analytical Data

  • Gene name

    ARF5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ADP-ribosylation factor 5; ARF5

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    AAP36805

  • Expression Region

    M1-R180

  • Protein Length

    Full Length

  • Molecular Weight

    22 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

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Protein Description

ARF5 (ADP-ribosylation factor 5) is a member of the ARF family of small GTPases, which play critical roles in regulating intracellular trafficking, cytoskeletal dynamics, and cellular signaling. Research on ARF5 has garnered significant interest due to its involvement in various cellular processes, including vesicle formation, membrane fusion, and endocytosis, which are essential for maintaining cellular homeostasis. Furthermore, ARF5 has been linked to important physiological functions, such as cell growth, differentiation, and stress responses, as well as pathological conditions like cancer and neurodegenerative diseases. The manipulation of ARF5 through recombinant protein technology has emerged as a valuable tool in elucidating its functional mechanisms and interactions within the cell. By producing and studying ARF5 recombinant proteins, researchers can investigate its GTPase activity, binding partners, and structural dynamics in detail. Such studies contribute to our understanding of the molecular basis of ARF5's role in cellular processes, paving the way for potential therapeutic strategies targeting ARF5-related dysregulation in various diseases. With advancements in protein expression systems and purification techniques, the study of ARF5 recombinant proteins continues to provide insights into fundamental cellular biology and therapeutic avenues.

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